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Zinc in PDB 3v0c: 4.3 Angstrom Crystal Structure of An Inactive Bont/A (E224Q/R363A/Y366F)

Protein crystallography data

The structure of 4.3 Angstrom Crystal Structure of An Inactive Bont/A (E224Q/R363A/Y366F), PDB code: 3v0c was solved by S.Gu, S.Rumpel, J.Zhou, J.Strotmeier, H.Bigalke, K.Perry, C.B.Shoemaker, A.Rummel, R.Jin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.11 / 4.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 167.521, 167.521, 158.733, 90.00, 90.00, 120.00
R / Rfree (%) 32.2 / 34.9

Zinc Binding Sites:

The binding sites of Zinc atom in the 4.3 Angstrom Crystal Structure of An Inactive Bont/A (E224Q/R363A/Y366F) (pdb code 3v0c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the 4.3 Angstrom Crystal Structure of An Inactive Bont/A (E224Q/R363A/Y366F), PDB code: 3v0c:

Zinc binding site 1 out of 1 in 3v0c

Go back to Zinc Binding Sites List in 3v0c
Zinc binding site 1 out of 1 in the 4.3 Angstrom Crystal Structure of An Inactive Bont/A (E224Q/R363A/Y366F)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 4.3 Angstrom Crystal Structure of An Inactive Bont/A (E224Q/R363A/Y366F) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1313

b:0.9
occ:1.00
OE2 A:GLU262 2.3 0.1 1.0
NE2 A:HIS223 2.6 0.2 1.0
NE2 A:HIS227 2.8 0.5 1.0
OE1 A:GLU262 2.8 0.3 1.0
CD A:GLU262 2.9 0.6 1.0
CD2 A:HIS223 3.0 0.4 1.0
CD2 A:HIS227 3.1 0.6 1.0
CE1 A:HIS223 3.8 0.9 1.0
CE1 A:HIS227 4.0 0.6 1.0
NE2 A:GLN224 4.0 0.5 1.0
CG A:HIS223 4.2 0.8 1.0
CG A:GLU262 4.3 0.9 1.0
CG A:HIS227 4.3 0.0 1.0
ND1 A:HIS223 4.6 0.8 1.0
ND1 A:HIS227 4.7 0.7 1.0
CD A:GLN224 4.8 0.6 1.0
OE1 A:GLN224 5.0 0.1 1.0
CG2 A:THR265 5.0 0.1 1.0

Reference:

S.Gu, S.Rumpel, J.Zhou, J.Strotmeier, H.Bigalke, K.Perry, C.B.Shoemaker, A.Rummel, R.Jin. Botulinum Neurotoxin Is Shielded By Ntnha in An Interlocked Complex. Science V. 335 977 2012.
ISSN: ISSN 0036-8075
PubMed: 22363010
DOI: 10.1126/SCIENCE.1214270
Page generated: Wed Dec 16 04:55:25 2020

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